HA2U_MOUSE
ID HA2U_MOUSE Reviewed; 227 AA.
AC P14438;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=H-2 class II histocompatibility antigen, A-U alpha chain;
DE Flags: Fragment;
GN Name=H2-Aa;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6309407; DOI=10.1016/0092-8674(83)90147-2;
RA Benoist C.O., Mathis D.J., Kanter M.R., Williams V.E., McDevitt H.O.;
RT "Regions of allelic hypervariability in the murine A alpha immune response
RT gene.";
RL Cell 34:169-177(1983).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; K01926; AAA39623.1; -; mRNA.
DR PIR; PL0125; PL0125.
DR PDB; 1K2D; X-ray; 2.20 A; A=1-179.
DR PDB; 1U3H; X-ray; 2.42 A; C/G=1-179.
DR PDB; 2P24; X-ray; 2.15 A; A=1-190.
DR PDB; 2PXY; X-ray; 2.23 A; C=1-178.
DR PDB; 2Z31; X-ray; 2.70 A; C=1-178.
DR PDBsum; 1K2D; -.
DR PDBsum; 1U3H; -.
DR PDBsum; 2P24; -.
DR PDBsum; 2PXY; -.
DR PDBsum; 2Z31; -.
DR AlphaFoldDB; P14438; -.
DR SMR; P14438; -.
DR MINT; P14438; -.
DR MaxQB; P14438; -.
DR PeptideAtlas; P14438; -.
DR PRIDE; P14438; -.
DR ProteomicsDB; 271388; -.
DR MGI; MGI:95895; H2-Aa.
DR ChiTaRS; H2-Aa; mouse.
DR EvolutionaryTrace; P14438; -.
DR Proteomes; UP000000589; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0042613; C:MHC class II protein complex; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0023026; F:MHC class II protein complex binding; IBA:GO_Central.
DR GO; GO:0042605; F:peptide antigen binding; IDA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0019882; P:antigen processing and presentation; IDA:MGI.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IDA:MGI.
DR GO; GO:0048002; P:antigen processing and presentation of peptide antigen; IDA:MGI.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISO:MGI.
DR GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; IBA:GO_Central.
DR GO; GO:0050870; P:positive regulation of T cell activation; IBA:GO_Central.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IDA:MGI.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.10.320.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003597; Ig_C1-set.
DR InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR InterPro; IPR014745; MHC_II_a/b_N.
DR InterPro; IPR001003; MHC_II_a_N.
DR Pfam; PF07654; C1-set; 1.
DR Pfam; PF00993; MHC_II_alpha; 1.
DR SMART; SM00407; IGc1; 1.
DR SMART; SM00920; MHC_II_alpha; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF54452; SSF54452; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Disulfide bond; Glycoprotein; Immunity;
KW Membrane; MHC II; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN <1..227
FT /note="H-2 class II histocompatibility antigen, A-U alpha
FT chain"
FT /id="PRO_0000080749"
FT TOPO_DOM <1..189
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 85..177
FT /note="Ig-like C1-type"
FT REGION <1..82
FT /note="Alpha-1"
FT REGION 83..176
FT /note="Alpha-2"
FT REGION 177..189
FT /note="Connecting peptide"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 105..161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT NON_TER 1
FT STRAND 1..13
FT /evidence="ECO:0007829|PDB:2P24"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:2P24"
FT STRAND 17..24
FT /evidence="ECO:0007829|PDB:2P24"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:2P24"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:2P24"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:2P24"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:2P24"
FT HELIX 55..74
FT /evidence="ECO:0007829|PDB:2P24"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:2Z31"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:2P24"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:2P24"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:2P24"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:2P24"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:2P24"
FT STRAND 143..151
FT /evidence="ECO:0007829|PDB:2P24"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:2P24"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:2P24"
SQ SEQUENCE 227 AA; 25136 MW; D1B7FDF1B390C877 CRC64;
DHVGSYGIVV YQSPGDIGQY TFEFDGDELF YVDLDKKETI WMLPEFAQLR SFDPQGGLQN
IATGKHNLGV LTKRSNSTPA TNEAPQATVF PKSPVLLGQP NTLICFVDNI FPPVINITWL
RNSKSVADGV YETSFFVNRD YSFHKLSYLT FIPSDDDIYD CKVEHWGLEE PVLKHWEPEI
PAPMSELTET VVCALGLSVG LVGIVVGTIF IIQGLRSGGT SRHPGPL
